Reviewed, UniProtKB/Swiss-Prot P15692 (VEGFA_HUMAN)

Names and origin

Protein names

Recommended name:
    Vascular endothelial growth factor A
      Short name=VEGF-A
Alternative name(s):
    Vascular permeability factor
      Short name=VPF

Gene names

Name:	VEGFA
Synonyms:	VEGF

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	232 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis, and induces permeabilization of blood vessels. Binds to the VEGFR1/Flt-1 and VEGFR2/Kdr receptors, heparan sulfate and heparin. Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to VEGFR2/Kdr but doesn't activate downstream signaling pathways, doesn't activate angiogenesis and inhibits tumor growth. Ref.26 Ref.27
Subunit structure	Homodimer; disulfide-linked. Also found as heterodimer with PlGF By similarity.
Subcellular location	Secreted. Note: VEGF121 is acidic and freely secreted. VEGF165 is more basic, has heparin-binding properties and, although a signicant proportion remains cell-associated, most is freely secreted. VEGF189 is very basic, it is cell-associated after secretion and is bound avidly by heparin and the extracellular matrix, although it may be released as a soluble form by heparin, heparinase or plasmin.
Tissue specificity	The VEGF189, VEGF-165 and VEGF-121 isoforms are widely expressed, whereas the VEGF206 and VEGF-145 are uncommon.
Induction	Regulated by growth factors, cytokines, gonadotropins, nitric oxide, hypoxia, hypoglycemia and oncogenic mutations.
Sequence similarities	Belongs to the PDGF/VEGF growth factor family.
Sequence caution	The sequence CAC19512.2 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Angiogenesis Differentiation
Cellular component	Secreted
Coding sequence diversity	Alternative splicing
Domain	Signal
Ligand	Heparin-binding
Molecular function	Developmental protein Growth factor Mitogen
PTM	Acetylation Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	induction of positive chemotaxis Non-traceable author statement. Source: UniProtKB platelet-derived growth factor receptor signaling pathway Inferred from direct assay. Source: UniProtKB positive regulation of blood vessel endothelial cell migration Inferred from direct assay. Source: UniProtKB positive regulation of cell division Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of endothelial cell proliferation Inferred from direct assay. Source: UniProtKB positive regulation of leukocyte migration Traceable author statement. Source: UniProtKB positive regulation of vascular endothelial growth factor receptor signaling pathway Inferred from direct assay. Source: UniProtKB regulation of cell shape Inferred from direct assay. Source: UniProtKB response to hypoxia Inferred from direct assay. Source: UniProtKB vasculogenesis Traceable author statement. Source: UniProtKB
Cellular component	cell surface Inferred from direct assay. Source: UniProtKB extracellular space Inferred from direct assay. Source: UniProtKB membrane Inferred from electronic annotation. Source: InterPro platelet alpha granule lumen Inferred from Experiment. Source: Reactome
Molecular function	cell surface binding Inferred from direct assay. Source: UniProtKB cytokine activity Inferred from sequence or structural similarity. Source: UniProtKB extracellular matrix binding Inferred by curator. Source: UniProtKB fibronectin binding Inferred from direct assay. Source: UniProtKB growth factor activity Inferred from direct assay. Source: UniProtKB heparin binding Inferred from direct assay. Source: UniProtKB platelet-derived growth factor receptor binding Inferred from physical interaction. Source: UniProtKB protein heterodimerization activity Inferred from direct assay. Source: MGI protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB vascular endothelial growth factor receptor 1 binding Inferred from physical interaction. Source: UniProtKB vascular endothelial growth factor receptor 2 binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NRP1	O14786	1	EBI-1026643,EBI-1187100

Alternative products

This entry describes 10 isoforms produced by alternative splicing. [Align] [Select]

Isoform VEGF206 (identifier: P15692-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform VEGF189 (identifier: P15692-2)

The sequence of this isoform differs from the canonical sequence as follows:
     166-182: Missing.

Isoform VEGF183 (identifier: P15692-3)

The sequence of this isoform differs from the canonical sequence as follows:
     160-182: Missing.

Isoform VEGF165 (identifier: P15692-4)

Also known as: VEGF;

The sequence of this isoform differs from the canonical sequence as follows:
     141-141: K → N
     142-182: Missing.

Isoform VEGF148 (identifier: P15692-5)

The sequence of this isoform differs from the canonical sequence as follows:
     141-141: K → N
     142-182: Missing.
     215-215: A → M
     216-232: Missing.

Isoform VEGF145 (identifier: P15692-6)

The sequence of this isoform differs from the canonical sequence as follows:
     166-226: Missing.

Isoform VEGF121 (identifier: P15692-7)

The sequence of this isoform differs from the canonical sequence as follows:
     141-141: K → N
     142-226: Missing.

Note: No experimental confirmation available.

Isoform VEGF165B (identifier: P15692-8)

The sequence of this isoform differs from the canonical sequence as follows:
     141-141: K → N
     142-182: Missing.
     227-232: CDKPRR → SLTRKD

Isoform VEGF121B (identifier: P15692-9)

The sequence of this isoform differs from the canonical sequence as follows:
     142-226: Missing.

Note: No experimental confirmation available.

Isoform VEGF111 (identifier: P15692-10)

The sequence of this isoform differs from the canonical sequence as follows:
     132-226: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Ref.22 Ref.23 Ref.24

Chain

27 – 232

206

Vascular endothelial growth factor A

PRO_0000023386

Amino acid modifications

Modified residue

147

1

N6-acetyllysine Ref.28

Modified residue

149

1

N6-acetyllysine Ref.28

Modified residue

152

1

N6-acetyllysine Ref.28

Glycosylation

101

1

N-linked (GlcNAc...)

Disulfide bond

52 ↔ 94

Disulfide bond

77

Interchain

Disulfide bond

83 ↔ 128

Disulfide bond

86

Interchain

Disulfide bond

87 ↔ 130

Natural variations

Alternative sequence

132 – 226

95

Missing in isoform VEGF111.

VSP_026781

Alternative sequence

141

1

K → N in isoform VEGF121, isoform VEGF148, isoform VEGF165 and isoform VEGF165B.

VSP_004618

Alternative sequence

142 – 226

85

Missing in isoform VEGF121 and isoform VEGF121B.

VSP_004620

Alternative sequence

142 – 182

41

Missing in isoform VEGF148, isoform VEGF165 and isoform VEGF165B.

VSP_004619

Alternative sequence

160 – 182

23

Missing in isoform VEGF183.

VSP_004621

Alternative sequence

166 – 226

61

Missing in isoform VEGF145.

VSP_004623

Alternative sequence

166 – 182

17

Missing in isoform VEGF189.

VSP_004622

Alternative sequence

215

1

A → M in isoform VEGF148.

VSP_004624

Alternative sequence

216 – 232

17

Missing in isoform VEGF148.

VSP_004625

Alternative sequence

227 – 232

6

CDKPRR → SLTRKD in isoform VEGF165B.

VSP_014783

Experimental info

Sequence conflict

87

1

C → S in AAC63143. Ref.8

Sequence conflict

210

1

D → H in AAC63143. Ref.8

Secondary structure

1

.

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.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

232

Helix Strand Turn

Details...

Helix

43 – 50

8

Beta strand

51 – 60

10

Helix

61 – 64

4

Helix

66 – 68

3

Beta strand

71 – 84

14

Beta strand

93 – 109

17

Beta strand

116 – 131

16

Beta strand

189 – 191

3

Beta strand

195 – 197

3

Turn

199 – 201

3

Beta strand

204 – 208

5

Helix

210 – 214

5

Turn

215 – 217

3

Beta strand

219 – 221

3

Turn

222 – 225

4

Beta strand

226 – 228

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform VEGF206 [UniParc]. Last modified November 16, 2001. Version 2. Checksum: FB49F364446F4D01	FASTA	232	27,042
	10 20 30 40 50 60 MNFLLSWVHW SLALLLYLHH AKWSQAAPMA EGGGQNHHEV VKFMDVYQRS YCHPIETLVD 70 80 90 100 110 120 IFQEYPDEIE YIFKPSCVPL MRCGGCCNDE GLECVPTEES NITMQIMRIK PHQGQHIGEM 130 140 150 160 170 180 SFLQHNKCEC RPKKDRARQE KKSVRGKGKG QKRKRKKSRY KSWSVYVGAR CCLMPWSLPG 190 200 210 220 230 PHPCGPCSER RKHLFVQDPQ TCKCSCKNTD SRCKARQLEL NERTCRCDKP RR
	Isoform VEGF189. Checksum: 7B9759AD5871FF33	FASTA	215	25,173
	10 20 30 40 50 60 MNFLLSWVHW SLALLLYLHH AKWSQAAPMA EGGGQNHHEV VKFMDVYQRS YCHPIETLVD 70 80 90 100 110 120 IFQEYPDEIE YIFKPSCVPL MRCGGCCNDE GLECVPTEES NITMQIMRIK PHQGQHIGEM 130 140 150 160 170 180 SFLQHNKCEC RPKKDRARQE KKSVRGKGKG QKRKRKKSRY KSWSVPCGPC SERRKHLFVQ 190 200 210 DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR
	Isoform VEGF183. Checksum: F01CCEACD945D6CA	FASTA	209	24,422
	10 20 30 40 50 60 MNFLLSWVHW SLALLLYLHH AKWSQAAPMA EGGGQNHHEV VKFMDVYQRS YCHPIETLVD 70 80 90 100 110 120 IFQEYPDEIE YIFKPSCVPL MRCGGCCNDE GLECVPTEES NITMQIMRIK PHQGQHIGEM 130 140 150 160 170 180 SFLQHNKCEC RPKKDRARQE KKSVRGKGKG QKRKRKKSRP CGPCSERRKH LFVQDPQTCK 190 200 CSCKNTDSRC KARQLELNER TCRCDKPRR
	Isoform VEGF165 (VEGF). Checksum: CCE57097DD3779BD	FASTA	191	22,314
	10 20 30 40 50 60 MNFLLSWVHW SLALLLYLHH AKWSQAAPMA EGGGQNHHEV VKFMDVYQRS YCHPIETLVD 70 80 90 100 110 120 IFQEYPDEIE YIFKPSCVPL MRCGGCCNDE GLECVPTEES NITMQIMRIK PHQGQHIGEM 130 140 150 160 170 180 SFLQHNKCEC RPKKDRARQE NPCGPCSERR KHLFVQDPQT CKCSCKNTDS RCKARQLELN 190 ERTCRCDKPR R
	Isoform VEGF148. Checksum: AE88400CA7757644	FASTA	174	20,218
	10 20 30 40 50 60 MNFLLSWVHW SLALLLYLHH AKWSQAAPMA EGGGQNHHEV VKFMDVYQRS YCHPIETLVD 70 80 90 100 110 120 IFQEYPDEIE YIFKPSCVPL MRCGGCCNDE GLECVPTEES NITMQIMRIK PHQGQHIGEM 130 140 150 160 170 SFLQHNKCEC RPKKDRARQE NPCGPCSERR KHLFVQDPQT CKCSCKNTDS RCKM
	Isoform VEGF145. Checksum: D02ECA735FF6E9F8	FASTA	171	20,064
	10 20 30 40 50 60 MNFLLSWVHW SLALLLYLHH AKWSQAAPMA EGGGQNHHEV VKFMDVYQRS YCHPIETLVD 70 80 90 100 110 120 IFQEYPDEIE YIFKPSCVPL MRCGGCCNDE GLECVPTEES NITMQIMRIK PHQGQHIGEM 130 140 150 160 170 SFLQHNKCEC RPKKDRARQE KKSVRGKGKG QKRKRKKSRY KSWSVCDKPR R
	Isoform VEGF121. Checksum: DDF4D6994249B9A6	FASTA	147	17,205
	10 20 30 40 50 60 MNFLLSWVHW SLALLLYLHH AKWSQAAPMA EGGGQNHHEV VKFMDVYQRS YCHPIETLVD 70 80 90 100 110 120 IFQEYPDEIE YIFKPSCVPL MRCGGCCNDE GLECVPTEES NITMQIMRIK PHQGQHIGEM 130 140 SFLQHNKCEC RPKKDRARQE NCDKPRR
	Isoform VEGF165B. Checksum: D25243E540AC79BD	FASTA	191	22,259
	10 20 30 40 50 60 MNFLLSWVHW SLALLLYLHH AKWSQAAPMA EGGGQNHHEV VKFMDVYQRS YCHPIETLVD 70 80 90 100 110 120 IFQEYPDEIE YIFKPSCVPL MRCGGCCNDE GLECVPTEES NITMQIMRIK PHQGQHIGEM 130 140 150 160 170 180 SFLQHNKCEC RPKKDRARQE NPCGPCSERR KHLFVQDPQT CKCSCKNTDS RCKARQLELN 190 ERTCRSLTRK D
	Isoform VEGF121B. Checksum: DDF4D6994249BED6	FASTA	147	17,219
	10 20 30 40 50 60 MNFLLSWVHW SLALLLYLHH AKWSQAAPMA EGGGQNHHEV VKFMDVYQRS YCHPIETLVD 70 80 90 100 110 120 IFQEYPDEIE YIFKPSCVPL MRCGGCCNDE GLECVPTEES NITMQIMRIK PHQGQHIGEM 130 140 SFLQHNKCEC RPKKDRARQE KCDKPRR
	Isoform VEGF111. Checksum: 196B2BB49381BE87	FASTA	137	15,981
	10 20 30 40 50 60 MNFLLSWVHW SLALLLYLHH AKWSQAAPMA EGGGQNHHEV VKFMDVYQRS YCHPIETLVD 70 80 90 100 110 120 IFQEYPDEIE YIFKPSCVPL MRCGGCCNDE GLECVPTEES NITMQIMRIK PHQGQHIGEM 130 SFLQHNKCEC RCDKPRR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Vascular endothelial growth factor is a secreted angiogenic mitogen." Leung D.W., Cachianes G., Kuang W.-J., Goeddel D.V., Ferrara N. Science 246:1306-1309(1989) [PubMed: 2479986] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS VEGF189 AND VEGF165).
[2]	"Vascular permeability factor, an endothelial cell mitogen related to PDGF." Keck P.J., Hauser S.D., Krivi G., Sanzo K., Warren T., Feder J., Connolly D.T. Science 246:1309-1312(1989) [PubMed: 2479987] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF189), PARTIAL PROTEIN SEQUENCE.
[3]	"The human gene for vascular endothelial growth factor. Multiple protein forms are encoded through alternative exon splicing." Tischer E., Mitchell R., Hartman T., Silva M., Gospodarowicz D., Fiddes J.C., Abraham J.A. J. Biol. Chem. 266:11947-11954(1991) [PubMed: 1711045] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM VEGF189).
[4]	"The vascular endothelial growth factor family: identification of a fourth molecular species and characterization of alternative splicing of RNA." Houck K.A., Ferrara N., Winer J., Cachianes G., Li B., Leung D.W. Mol. Endocrinol. 5:1806-1814(1991) [PubMed: 1791831] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM VEGF206).
[5]	"AIDS-associated Kaposi's sarcoma cells in culture express vascular endothelial growth factor." Weindel K., Marme D., Weich H.A. Biochem. Biophys. Res. Commun. 183:1167-1174(1992) [PubMed: 1567395] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
[6]	"VEGF145, a secreted vascular endothelial growth factor isoform that binds to extracellular matrix." Poltorak Z., Cohen T., Sivan R., Kandelis Y., Spira G., Vlodavsky I., Keshet E., Neufeld G. J. Biol. Chem. 272:7151-7158(1997) [PubMed: 9054410] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF145).
[7]	"Identification and characterization of a new splicing variant of vascular endothelial growth factor: VEGF183." Lei J., Jiang A., Pei D. Biochim. Biophys. Acta 1443:400-406(1998) [PubMed: 9878851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF183). Tissue: Kidney.
[8]	"Identification of a human VPF/VEGF 3' untranslated region mediating hypoxia-induced mRNA stability." Claffey K.P., Shih S.-C., Mullen A., Dziennis S., Cusick J.L., Abrams K.R., Lee S.W., Detmar M. Mol. Biol. Cell 9:469-481(1998) [PubMed: 9450968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165). Tissue: Mammary gland.
[9]	"Heterogeneous vascular endothelial growth factor (VEGF) isoform mRNA and receptor mRNA expression in human glomeruli, and the identification of VEGF148 mRNA, a novel truncated splice variant." Whittle C.J., Gillespie K.M., Harrison R., Mathieson P.W., Harper S.J. Clin. Sci. 97:303-312(1999) [PubMed: 10464055] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF148). Tissue: Renal glomerulus.
[10]	"VEGF165b, an inhibitory splice variant of vascular endothelial growth factor, is down-regulated in renal cell carcinoma." Bates D.O., Cui T.-G., Doughty J.M., Winkler M., Sugiono M., Shields J.D., Peat D., Gillatt D., Harper S.J. Cancer Res. 62:4123-4131(2002) [PubMed: 12124351] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165B). Tissue: Kidney.
[11]	"Human cDNA for the vascular endothelial growth factor isoform VEGF165." Murata H., Fukushima J., Hattori S., Okuda K., Yanagi H. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165). Tissue: Hemangioendothelioma.
[12]	"Human cDNA for vascular endothelial growth factor isoform VEGF121." Sato J.D., Whitney R.G. Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF121).
[13]	"Cloning of vascular endothelial growth factor (VEGF) cDNA." Liu J., Peng X., Yuan J., Qiang B. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
[14]	"Cloning and identification of vascular endothelial growth factor isoform VEGF165." Shan Z.X., Yu X.Y., Lin Q.X., Fu Y.H., Zheng M., Tan H.H., Lin S.G. Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165). Tissue: Heart.
[15]	"Cloning and characterization of VEGF from LnCAP cells, a line of prostate cancer cells." Koul S., Johnson T., Meacham R.B., Koul H.K. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
[16]	"VEGF111, a new VEGF-A variant lacking exons 5, 6 and 7." Mineur P.J., Colige A.C., Lambert C.A. Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF111).
[17]	"Human protein factory for converting the transcriptome into an in vitro-expressed proteome." Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N. Nat. Methods 5:1011-1017(2008) [PubMed: 19054851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM VEGF165).
[18]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[19]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[20]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM VEGF121B). Tissue: Lung.
[21]	SeattleSNPs variation discovery resource Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-232.
[22]	"Synthesis and assembly of functionally active human vascular endothelial growth factor homodimers in insect cells." Fiebich B.L., Jaeger B., Schoellmann C., Weindel K., Wilting J., Kochs G., Marme D., Hug H., Weich H.A. Eur. J. Biochem. 211:19-26(1993) [PubMed: 7678805] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-41.
[23]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-41.
[24]	"Human vascular permeability factor. Isolation from U937 cells." Connolly D.T., Olander J.V., Heuvelman D., Nelson R., Monsell R., Siegel N., Haymore B.L., Leimgruber R., Feder J. J. Biol. Chem. 264:20017-20024(1989) [PubMed: 2584205] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE OF 27-36; 43-50 AND 59-81.
[25]	"Human Muller cells express VEGF183, a novel spliced variant of vascular endothelial growth factor." Jingjing L., Xue Y., Agarwal N., Roque R.S. Invest. Ophthalmol. Vis. Sci. 40:752-759(1999) [PubMed: 10067980] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 114-209 (ISOFORM VEGF183). Tissue: Retina.
[26]	"Vascular endothelial growth factor induces cyclooxygenase-dependent proliferation of endothelial cells via the VEGF-2 receptor." Murphy J.F., Fitzgerald D.J. FASEB J. 15:1667-1669(2001) [PubMed: 11427521] [Abstract] Cited for: FUNCTION.
[27]	"VEGF165b, an inhibitory vascular endothelial growth factor splice variant: mechanism of action, in vivo effect on angiogenesis and endogenous protein expression." Woolard J., Wang W.-Y., Bevan H.S., Qiu Y., Morbidelli L., Pritchard-Jones R.O., Cui T.-G., Sugiono M., Waine E., Perrin R., Foster R., Digby-Bell J., Shields J.D., Whittles C.E., Mushens R.E., Gillatt D.A., Ziche M., Harper S.J., Bates D.O. Cancer Res. 64:7822-7835(2004) [PubMed: 15520188] [Abstract] Cited for: FUNCTION (ISOFORM VEGF165B).
[28]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147; LYS-149 AND LYS-152, MASS SPECTROMETRY. Tissue: Epithelium.
[29]	"Vascular endothelial growth factor: crystal structure and functional mapping of the kinase domain receptor binding site." Muller Y.A., Li B., Christinger H.W., Wells J.A., Cunningham B.C., de Vos A.M. Proc. Natl. Acad. Sci. U.S.A. 94:7192-7197(1997) [PubMed: 9207067] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 34-135.
[30]	"1H, 13C, and 15N backbone assignment and secondary structure of the receptor-binding domain of vascular endothelial growth factor." Fairbrother W.J., Champe M.A., Christinger H.W., Keyt B.A., Starovasnik M.A. Protein Sci. 6:2250-2260(1997) [PubMed: 9336848] [Abstract] Cited for: STRUCTURE BY NMR OF 34-135.
[31]	"The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93-A resolution: multiple copy flexibility and receptor binding." Muller Y.A., Christinger H.W., Keyt B.A., de Vos A.M. Structure 5:1325-1338(1997) [PubMed: 9351807] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 34-135.
[32]	"Crystal structure of the complex between VEGF and a receptor-blocking peptide." Wiesmann C., Christinger H.W., Cochran A.G., Cunningham B.C., Fairbrother W.J., Keenan C.J., Meng G., de Vos A.M. Biochemistry 37:17765-17772(1998) [PubMed: 9922142] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 39-134.
[33]	"Solution structure of the heparin-binding domain of vascular endothelial growth factor." Fairbrother W.J., Champe M.A., Christinger H.W., Keyt B.A., Starovasnik M.A. Structure 6:637-648(1998) [PubMed: 9634701] [Abstract] Cited for: STRUCTURE BY NMR OF 137-215.
+	Additional computationally mapped references.

Web resources

R&D Systems' cytokine mini-reviews: VEGF

Wikipedia

VEGF entry

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M32977 mRNA. Translation: AAA35789.1.
M27281 mRNA. Translation: AAA36807.1.
M63978 , M63971, M63972, M63973, M63974, M63975, M63976, M63977 Genomic DNA. Translation: AAA36804.1.
S85192 mRNA. Translation: AAC63102.1. Different initiation.
S85224 , S85199, S85201, S85219, S85222 Genomic DNA. Translation: AAC63101.1.
X62568 mRNA. Translation: CAA44447.1.
AJ010438 mRNA. Translation: CAA09179.1.
AF022375 mRNA. Translation: AAC63143.1.
AF091352 mRNA. Translation: AAD55345.1.
AF430806 mRNA. Translation: AAL27435.1.
AB021221 mRNA. Translation: BAA78418.1.
AF214570 mRNA. Translation: AAF19659.1.
AY047581 mRNA. Translation: AAK95847.1.
AF486837 mRNA. Translation: AAM03108.1.
AY766116 mRNA. Translation: AAV34601.1.
DQ229900 mRNA. Translation: ABB58912.1.
AB451322 mRNA. Translation: BAG70136.1.
AB451451 mRNA. Translation: BAG70265.1.
AL136131 Genomic DNA. Translation: CAC19512.2. Sequence problems.
AL136131 Genomic DNA. Translation: CAC19513.2.
AL136131 Genomic DNA. Translation: CAC19515.2.
AL136131 Genomic DNA. Translation: CAC19516.2. Different initiation.
CH471081 Genomic DNA. Translation: EAX04229.1.
BC065522 mRNA. Translation: AAH65522.2. Different initiation.
AF437895 Genomic DNA. Translation: AAL27630.1.
AF062645 mRNA. Translation: AAC16730.1.

IPI

IPI00012567.
IPI00064652.
IPI00216554.
IPI00216555.
IPI00374772.
IPI00607783.
IPI00607893.
IPI00852889.
IPI00872936.
IPI00940477.

PIR

A41551.

RefSeq

NP_001020537.2.
NP_001020538.2.
NP_001020539.2.
NP_001020540.2.
NP_001020541.2.
NP_001028928.1.
NP_003367.4.

UniGene

Hs.73793

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BJ1	X-ray	2.40	V/W	34-135	[»]
1CZ8	X-ray	2.40	V/W	40-133	[»]
1FLT	X-ray	1.70	V/W	38-135	[»]
1KAT	NMR	-	V/W	37-135	[»]
1KMX	NMR	-	A	183-232	[»]
1MJV	X-ray	2.10	A/B	40-134	[»]
1MKG	X-ray	2.50	A/B/C/D	40-134	[»]
1MKK	X-ray	1.32	A/B	40-134	[»]
1QTY	X-ray	2.70	R/S/V/W	34-135	[»]
1TZH	X-ray	2.60	V/W	34-135	[»]
1TZI	X-ray	2.80	V	34-135	[»]
1VGH	NMR	-	A	183-232	[»]
1VPF	X-ray	2.50	A/B/C/D	34-135	[»]
1VPP	X-ray	1.90	V/W	34-135	[»]
2FJG	X-ray	2.80	V/W	34-135	[»]
2FJH	X-ray	3.10	V/W	34-135	[»]
2QR0	X-ray	3.50	C/D/I/J/O/P/U/V	39-135	[»]
2VGH	NMR	-	A	183-232	[»]
2VPF	X-ray	1.93	A/B/C/D/E/F/G/H	34-135	[»]
3BDY	X-ray	2.60	V	34-135	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-165N.
DIP-5740N.
DIP-5742N.

IntAct

P15692. 2 interactions.

STRING

P15692.

PTM databases

PhosphoSite

P15692.

Genome annotation databases

Ensembl

ENST00000372055; ENSP00000361125; ENSG00000112715; Homo sapiens. [Genome view]

GeneID

7422.

KEGG

hsa:7422.

UCSC

uc003owc.1. human.
uc003owe.1. human.
uc003owf.1. human.
uc003owg.1. human.
uc003owh.1. human.
uc003owi.1. human.

Organism-specific databases

CTD

7422.

GeneCards

GC06P043846.

H-InvDB

HIX0005915.

HGNC

HGNC:12680. VEGFA.

MIM

192240. gene.

PharmGKB

PA37302.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P15692.

InParanoid

P15692.

Enzyme and pathway databases

Pathway_Interaction_DB

glypican_1pathway. Glypican 1 network.
hif1_tfpathway. HIF-1-alpha transcription factor network.
avb3_integrin_pathway. Integrins in angiogenesis.
s1p_s1p1_pathway. S1P1 pathway.
s1p_s1p3_pathway. S1P3 pathway.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
vegfr1_pathway. VEGFR1 specific signals.

Reactome

REACT_12529. Signaling by VEGF.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P15692.

Bgee

P15692.

Genevestigator

P15692.

GermOnline

ENSG00000112715. Homo sapiens.

Family and domain databases

InterPro

IPR000072. PD_growth_factor.
[Graphical view]

Pfam

PF00341. PDGF. 1 hit.
[Graphical view]

SMART

SM00141. PDGF. 1 hit.
[Graphical view]

PROSITE

PS00249. PDGF_1. 1 hit.
PS50278. PDGF_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB01076. Atorvastatin.
DB00112. Bevacizumab.
DB01136. Carvedilol.
DB01381. Ginkgo biloba.
DB01120. Gliclazide.
DB01017. Minocycline.
DB01270. Ranibizumab.
DB00641. Simvastatin.

NextBio

29060.

SOURCE

Search...

Entry information

Entry name

VEGFA_HUMAN

Accession

Primary (citable) accession number: P15692
Secondary accession number(s): B5BU86 , O60720, O75875, Q074Z4, Q16889, Q5UB46, Q6P0P5, Q96KJ0, Q96L82, Q96NW5, Q9H1W8, Q9H1W9, Q9UH58, Q9UL23

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	November 16, 2001
Last modified:	February 9, 2010
This is version 145 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.